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Enzymatic and microenvironmental regulation in adenosine metabolism-mediated immunosuppression. [PDF]
Front ImmunolLi C, Chen L, Li Z, Liang L, Lou B.
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Clinical Biochemistry, 1970
Summary 1. Sequential studies of serum 5′-nucleotidase (EC 3.1.3.5) in association with other enzymes in patients with malignant diseases are presented. 2. Evidence is given for the specific significance of the assay of 5′-nucleotidase in serum which is a sensitive monitor for the appearance of metastases in liver. 3.
W, van der Slik +3 more
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Summary 1. Sequential studies of serum 5′-nucleotidase (EC 3.1.3.5) in association with other enzymes in patients with malignant diseases are presented. 2. Evidence is given for the specific significance of the assay of 5′-nucleotidase in serum which is a sensitive monitor for the appearance of metastases in liver. 3.
W, van der Slik +3 more
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Archives of Biochemistry and Biophysics, 1994
The cytosolic 5'-nucleotidase specific for IMP, GMP, and their deoxyderivatives has been purified approximately 1000 times from calf thymus. The enzyme, in the presence of a suitable nucleoside, can act as a phosphotransferase, catalyzing the transfer of the phosphate moiety from a nucleoside monophosphate donor to a nucleoside acceptor, thus operating
PESI, ROSSANA +6 more
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The cytosolic 5'-nucleotidase specific for IMP, GMP, and their deoxyderivatives has been purified approximately 1000 times from calf thymus. The enzyme, in the presence of a suitable nucleoside, can act as a phosphotransferase, catalyzing the transfer of the phosphate moiety from a nucleoside monophosphate donor to a nucleoside acceptor, thus operating
PESI, ROSSANA +6 more
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The 5′-Nucleotidases and Cyclic Phosphodiesterases (3′-Nucleotidases) of the Enterobacteriaceae
Journal of Bacteriology, 1968All members of the Enterobacteriaceae possess distinct 5′-nucleotidases and cyclic phosphodiesterases (3′-nucleotidases) that can be differentiated from the acid and alkaline phosphatases and the acid sugar hydrolases. The nucleotidases and cyclic phosphodiesterases of the various Enterobacteriaceae
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Diphosphopyridine Nucleotidase and Acute Glomerulonephritis
Archives of Internal Medicine, 1962The presence of diphosphopyridine nucleotidase (DPNase) in filtrates of cultures of hemolytic streptococci was first described in 1956. 1,2 Among several bacterial species studied, only streptococci of Groups A, C, and G produced this extracellular enzyme.
A J, GONZAGA, C H, RAMMELKAMP
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5′-nucleotidase of chicken liver
Biochimica et Biophysica Acta (BBA) - Enzymology, 19671. 1.|5′-Nucleotidase (5′-ribonucleotide phosphophydrolase, EC 3.1.3.5) was partially purified from chicken liver. This is the first time it has been possible to obtain 5′-nucleotidase from the hepatic tissue of uricotelic animals and it was found to be kinetically distinct from 5′-nucleotidases obtained from other sources. 2.
R, Itoh, A, Mitsui, K, Tsushima
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Erythrocyte Pyrimidine 5′‐Nucleotidase
British Journal of Haematology, 1980Summary In this study 31 family members of a patient with erythrocyte pyrimidine 5′‐nucleotidase deficiency were studied. The activity of this enzyme in their erythrocytes is compared with levels in normal subjects and the problems surrounding heterozygote detection are discussed.
J D, Torrance, D, Whittaker, T, Jenkins
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The Histochemical Journal, 1969
Under assay conditions such that there is minimal interference by lysosomal acid phosphatase, the dephosphorylation of nucleoside-5′-monophosphates (AMP or UMP) by rat-liver homogenates at alkaline pH values is attributable to a Mg2+-dependent enzyme (5′-nucleotidase, EC 3.1.3.5).
A A, el-Aaser, E, Reid
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Under assay conditions such that there is minimal interference by lysosomal acid phosphatase, the dephosphorylation of nucleoside-5′-monophosphates (AMP or UMP) by rat-liver homogenates at alkaline pH values is attributable to a Mg2+-dependent enzyme (5′-nucleotidase, EC 3.1.3.5).
A A, el-Aaser, E, Reid
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5-Nucleotidase activity in lymphocytes
The Histochemical Journal, 1981Some characteristics of lymphocyte 5'-nucleotidase are reviewed. The optimal conditions for the cytochemical localization of 5'-nucleotidase (AMPase) in the mouse lymphocyte have been established. Quantitative monitoring of the effects of fixation and the components of the cytochemical medium showed that cytochemistry can be performed under conditions ...
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Micrococcus radiodurans 5′-nucleotidase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1973Abstract A 5′-nucleotidase (5′-ribonucleotide phosphohydrolase, EC 3.1.3.5) isolated from Micrococcus radiodurans appears to have properties more closely resembling some of the corresponding vertebrate enzymes than the reported bacterial enzymes. The M. radiodurans enzyme is a strict nucleoside 5′-phosphomonoesterase with a pH optimum between 8 and 9.
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